title: A Golgi and tonoplast localized S-acyl transferase is involved in cell expansion, cell division, vascular patterning and fertility in Arabidopsis.
abstract: S-acylation of eukaryotic proteins is the reversible attachment of palmitic or stearic acid to cysteine residues, catalysed by protein S-acyl transferases that share an Asp-His-His-Cys (DHHC) motif. Previous evidence suggests that in Arabidopsis S-acylation is involved in the control of cell size, polarity and the growth of pollen tubes and root hairs. Using a combination of yeast genetics, biochemistry, cell biology and loss of function genetics the roles of a member of the protein S-acyl transferase PAT family, AtPAT10 (At3g51390), have been explored. In keeping with its role as a PAT, AtPAT10 auto-S-acylates, and partially complements the yeast akr1 PAT mutant, and this requires Cys(192) of the DHHC motif. In Arabidopsis AtPAT10 is localized in the Golgi stack, trans-Golgi network/early endosome and tonoplast. Loss-of-function mutants have a pleiotropic phenotype involving cell expansion and division, vascular patterning, and fertility that is rescued by wild-type AtPAT10 but not by catalytically inactive AtPAT10C(192) A. This supports the hypothesis that AtPAT10 is functionally independent of the other Arabidopsis PATs. Our findings demonstrate a growing importance of protein S-acylation in plants, and reveal a Golgi and tonoplast located S-acylation mechanism that affects a range of events during growth and development in Arabidopsis.
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.|State Key Laboratory of Crop Biology, Shandong Agricultural University, Shandong, 271018, China.
authors.forename: Baoxiu
authors.initials: B
authors.lastname: Qi
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.
authors.forename: James
authors.initials: J
authors.lastname: Doughty
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.
authors.forename: Richard
authors.initials: R
authors.lastname: Hooley
mesh_terms: D000215:Acylation; D000217:Acyltransferases / Q000235:genetics* / Q000378:metabolism; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism; D002455:Cell Division; D005298:Fertility; D035264:Flowers / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D006056:Golgi Apparatus / Q000201:enzymology*; D016254:Mutagenesis, Insertional; D019308:Palmitic Acid / Q000378:metabolism; D010641:Phenotype; D018515:Plant Leaves / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D018517:Plant Roots / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D018520:Plant Shoots / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D030821:Plants, Genetically Modified; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D036226:Seedlings / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D012639:Seeds / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D013229:Stearic Acids / Q000378:metabolism; D014617:Vacuoles / Q000201:enzymology; D021601:trans-Golgi Network / Q000201:enzymology
chemical_list: D029681:Arabidopsis Proteins; D013229:Stearic Acids; D019308:Palmitic Acid; C031183:stearic acid; D000217:Acyltransferases; C587777:PAT10 protein, Arabidopsis
keywords: Arabidopsis; DHHC-PAT; Golgi; dwarfism; protein S-acylation; tonoplast; trans-Golgi network; vascular patterning